Limited enzymatically hydrolyzed pea protein–inulin interactions in gel systems

Gelation of protein-polysaccharide mixtures can help create a variety of distinctive gel systems as compared to single polysaccharide or protein gels. The properties of these functional gels are heavily reliant upon the nature of protein-polysaccharides interactions, their gelling compatibility, and mechanism. Pea protein isolate dispersions (7.5%) were subjected to limited enzymatic hydrolysis using the enzyme Alcalase<sup>®</sup> at three hydrolysis times (0, 3, and 6 min). Inulin was added according to three ratios (0, 1:4, and 2:4) with pea protein. Viscoelastic properties of the gels formed were measured using amplitude sweep and frequency sweep. Storage modulus (G') measurements from the amplitude sweep indicated that samples hydrolyzed for 3 min with 1:4 ratio of inulin to pea protein had maximum gel strength, exhibiting G' values of ∼307 Pa. G' values for samples hydrolyzed for 0 and 6 min with different inulin ratios averaged ∼13 and ∼144 Pa, respectively. Confocal laser scanning microscopy showed that gels developed by samples hydrolyzed for 3 min showed a dense network as compared to an open network in gels formed by samples hydrolyzed for 6 min, whereas large random aggregates were observed in gels formed by samples hydrolyzed for 0 min. The study confirmed that inulin promotes noncovalent bond formation in samples hydrolyzed for 3 min with a 1:4 inulin ratio, shown by an ∼18% increased protein solubility in urea. Additionally, collaboration between noncovalent bonds and disulfide linkages stabilized the gel structure, as indicated by further increase in solubility in combination of urea and Dithiothreitol. PRACTICAL APPLICATION: Plant proteins are gaining attention as alternatives to animal proteins. However, they have inferior functionality, which affects their applicability in food products. This investigation aimed to evaluate enzymatic hydrolysis to enhance the structural and functional properties of pea proteins, thus increasing their applicability in the food industry. Inulin is an oligosaccharide and soluble fiber, which promotes gut health. Thus, gels combining hydrolyzed pea protein and inulin can serve as a model mixed food system of interest to both the industry and consumers.

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Publication Details

Journal
Journal of Food Science
Published
2024-12-01
DOI
https://doi.org/10.1111/1750-3841.17581
Citations
4
Primary Topic
Protein Hydrolysis and Bioactive Peptides
Type
article
Field-Weighted Citation Impact
0.94
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article

Limited enzymatically hydrolyzed pea protein–inulin interactions in gel systems

Valente B. Alvárez, Sanjana Sawant, Dennis R. Heldman
4 citations
Journal of Food Science
Protein Hydrolysis and Bioactive Peptides
0.94
article

Limited enzymatically hydrolyzed pea protein–inulin interactions in gel systems

Valente B. Alvárez, Sanjana Sawant, Dennis R. Heldman
article en
4 citations

Abstract

Gelation of protein-polysaccharide mixtures can help create a variety of distinctive gel systems as compared to single polysaccharide or protein gels. The properties of these functional gels are heavily reliant upon the nature of protein-polysaccharides interactions, their gelling compatibility, and mechanism. Pea protein isolate dispersions (7.5%) were subjected to limited enzymatic hydrolysis using the enzyme Alcalase<sup>®</sup> at three hydrolysis times (0, 3, and 6 min). Inulin was added according to three ratios (0, 1:4, and 2:4) with pea protein. Viscoelastic properties of the gels formed were measured using amplitude sweep and frequency sweep. Storage modulus (G') measurements from the amplitude sweep indicated that samples hydrolyzed for 3 min with 1:4 ratio of inulin to pea protein had maximum gel strength, exhibiting G' values of ∼307 Pa. G' values for samples hydrolyzed for 0 and 6 min with different inulin ratios averaged ∼13 and ∼144 Pa, respectively. Confocal laser scanning microscopy showed that gels developed by samples hydrolyzed for 3 min showed a dense network as compared to an open network in gels formed by samples hydrolyzed for 6 min, whereas large random aggregates were observed in gels formed by samples hydrolyzed for 0 min. The study confirmed that inulin promotes noncovalent bond formation in samples hydrolyzed for 3 min with a 1:4 inulin ratio, shown by an ∼18% increased protein solubility in urea. Additionally, collaboration between noncovalent bonds and disulfide linkages stabilized the gel structure, as indicated by further increase in solubility in combination of urea and Dithiothreitol. PRACTICAL APPLICATION: Plant proteins are gaining attention as alternatives to animal proteins. However, they have inferior functionality, which affects their applicability in food products. This investigation aimed to evaluate enzymatic hydrolysis to enhance the structural and functional properties of pea proteins, thus increasing their applicability in the food industry. Inulin is an oligosaccharide and soluble fiber, which promotes gut health. Thus, gels combining hydrolyzed pea protein and inulin can serve as a model mixed food system of interest to both the industry and consumers.

Journal of Food ScienceVol. 89(12)
University of Wisconsin–Madison (US), The Ohio State University (US)
Openalex Percentile: Top 24%
Protein Hydrolysis and Bioactive Peptides
0.94
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